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Literature summary extracted from

  • Ma, Q.; Akhter, Y.; Wilmanns, M.; Ehebauer, M.T.
    Active site conformational changes upon reaction intermediate biotinyl-5-AMP binding in biotin protein ligase from Mycobacterium tuberculosis (2014), Protein Sci., 23, 932-939 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.3.4.15 structures of the apo-form and in complex with reaction intermediate biotinyl-5'-AMP. Binding of the reaction intermediate leads to clear disorder-to-order transitions. A conserved lysine, Lys138, in the active site is essential for biotinylation Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
6.3.4.15 K138S inactive Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.4.15 0.2
-
ATP pH 8.0, 30°C Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.15 Mycobacterium tuberculosis I6YFP0
-
-
6.3.4.15 Mycobacterium tuberculosis H37Rv I6YFP0
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.4.15 ATP + biotin + apo-[acetyl-CoA carbon-dioxide ligase]
-
Mycobacterium tuberculosis AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase]
-
?
6.3.4.15 ATP + biotin + apo-[acetyl-CoA carbon-dioxide ligase]
-
Mycobacterium tuberculosis H37Rv AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase]
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.3.4.15 0.017
-
ATP pH 8.0, 30°C Mycobacterium tuberculosis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.3.4.15 0.085
-
ATP pH 8.0, 30°C Mycobacterium tuberculosis